A rat liver protein with potential thrombin activity: Properties and partial purification

D. V. Shah, J. W. Suttie, G. A. Grant

Research output: Contribution to journalArticlepeer-review

29 Scopus citations

Abstract

A protein which generates thrombin activity when treated with the venom from Echis carinatus has been shown to build up in the liver microsomes of vitamin K-deficient or anticoagulant-treated rats. The amount of this protein decreases rapidly when vitamin K is given to these animals. The protein has been partially purified. It differs from prothrombin in its ability to adsorb to BaSO4, its electrophoretic mobility, and chromatography on DEAE-cellulose. It does, however, react with antibody prepared against rat prothrombin, and it apparently contains the thrombin portion of prothrombin. These observations are consistent with the hypothesis that this protein represents a liver precursor protein which is converted to plasma prothrombin in a vitamin K-dependent step.

Original languageEnglish
Pages (from-to)483-491
Number of pages9
JournalArchives of Biochemistry and Biophysics
Volume159
Issue number1
DOIs
StatePublished - Nov 1973

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